Information on EC 5.3.1.8 - Mannose-6-phosphate isomerase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY
5.3.1.8
-
RECOMMENDED NAME
GeneOntology No.
Mannose-6-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
analysis of enzyme-substrate and enzyme-inhibitor complexes by ESI-FTICR mass spectrometry
-
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
cis-enediol mechanism
-, Q8ZWV0
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
mechanism does not involve trans-enediol. Instead, activity may result from additional space in the active site which permits rotation of the C2-C3 bond
Q8ZWV0
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
hydride transfer mechanism of a alpha-hydrogen bond between the C1 and C2 positions of substrate. Mechanism involves Zn2+ mediating the movement of a proton between O1 and O2, and the hydrophobic environment formed in part by T278 promoting transfer of a hydride ion
-
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
reaction mechanism, overview. Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site. Isomerization probably follows a cis-enediol mechanism, overall folding pattern of the central catalytic domain, overview
P25081
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldose-ketose-isomerization
Q5SIM4
-
aldose-ketose-isomerization
Thermus thermophilus KCCM 40879
-
-
-
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
D-mannose degradation
-
Fructose and mannose metabolism
-
GDP-mannose biosynthesis
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
mannitol biosynthesis
-
mannitol degradation II
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
D-mannose-6-phosphate aldose-ketose-isomerase
A zinc protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
becA
Burkholderia cepacia IST408
Q06XM8
-
-
D-mannose-6-phosphate ketol-isomerase
-
-
-
-
Isomerase, mannose phosphate
-
-
-
-
ManA
Photorhabdus luminescens TT01
-
-
-
Mannose phosphate isomerase
-
-
-
-
mannose-6-phosphate isomerase
Q5SIM4
-
mannose-6-phosphate isomerase
Thermus thermophilus KCCM 40879
Q5SIM4
-
-
MPI
Thermus thermophilus KCCM 40879
-, Q5SIM4
-
-
PHM
Sulfolobus solfataricus P1
-
-
-
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
-
Phosphohexomutase
-
-
Phosphohexomutase
Sulfolobus solfataricus P1
-
-
-
Phosphomannoisomerase
-
-
-
-
Phosphomannose isomerase
-
-
-
-
Phosphomannose isomerase
-
-
Phosphomannose isomerase
Alcaligenes sp. CGMCC2428
-
-
-
Phosphomannose isomerase
Q9M884
-
Phosphomannose isomerase
Q66WM4
-
Phosphomannose isomerase
Aspergillus fumigatus YJ-407
Q66WM4
-
-
Phosphomannose isomerase
-
-
Phosphomannose isomerase
-
-
Phosphomannose isomerase
Photorhabdus luminescens TT01
-
-
-
Phosphomannose isomerase
-
-
Phosphomannose isomerase
-
type II phosphomannose isomerase, bifunctional phosphomannose isomerase/GDP-mannose pyrophosphorylase (manC), with both PMI (E.C. 5.3.1.8) and GMP (E.C.2.7.7.13) activities
Phosphomannose isomerase
-
-
Phosphomannose isomerase
-
-
Phosphomannose isomerase
Sphingobium chungbukense DJ77
-
-
-
phosphomannose-isomerase
-
-
phosphomannose-isomerase
Oncidium Gower Ramsey, Oncidium sp.
-
-
Phosphphexomutase
-
-
-
-
PMI
-
-
-
-
PMI
Alcaligenes sp. CGMCC2428
-
-
-
PMI
Oncidium Gower Ramsey, Oncidium sp.
-
-
PMI
Photorhabdus luminescens TT01
-
-
-
PMI
Sphingobium chungbukense DJ77
-
-
-
PMI/GMP
Sphingobium chungbukense DJ77
-
-
-
Pmi1
Aspergillus fumigatus YJ-407
Q66WM4
-
-
PslB
Pseudomonas aeruginosa PAO1.
-
-
-
type I phosphomannose isomerase
-
-
type I phosphomannose isomerases
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-88-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
Manually annotated by BRENDA team
strain CGMCC2428
-
-
Manually annotated by BRENDA team
Alcaligenes sp. CGMCC2428
strain CGMCC2428
-
-
Manually annotated by BRENDA team
isoform Pmi1; isoform Pmi2
-
-
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
strain YJ-407, gene pmi1
UniProt
Manually annotated by BRENDA team
Aspergillus fumigatus YJ-407
strain YJ-407, gene pmi1
UniProt
Manually annotated by BRENDA team
enzyme from Bacillus subtilis strain HB002; ATCC 23857
UniProt
Manually annotated by BRENDA team
different cultivars, gene pmi
-
-
Manually annotated by BRENDA team
strain J2315, bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
Manually annotated by BRENDA team
type II enzyme, bifunctional protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
SwissProt
Manually annotated by BRENDA team
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Cassia coluteoides
-
-
-
Manually annotated by BRENDA team
expression in Brassica rapa
-
-
Manually annotated by BRENDA team
expression in Linum usitatissimum
-
-
Manually annotated by BRENDA team
expression in Malus domestica
-
-
Manually annotated by BRENDA team
expression in onion
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Microorganisms
-
-
-
Manually annotated by BRENDA team
Oncidium sp.
-
-
-
Manually annotated by BRENDA team
Photorhabdus luminescens TT01
-
-
-
Manually annotated by BRENDA team
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase
-
-
Manually annotated by BRENDA team
strain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PAO1.
strain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
Manually annotated by BRENDA team
bifunctional phosphoglucose isomerase/phosphomannose isomerase, EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
Manually annotated by BRENDA team
bifunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.8 and EC 5.3.1.9, overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
Manually annotated by BRENDA team
secretory mutant with a thermolabile phosphomannose isomerase
-
-
Manually annotated by BRENDA team
strain DJ77, gene pmi
-
-
Manually annotated by BRENDA team
Sphingobium chungbukense DJ77
strain DJ77, gene pmi
-
-
Manually annotated by BRENDA team
strain P1 (ATCC 35091)
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus P1
strain P1 (ATCC 35091)
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
Manually annotated by BRENDA team
Thermus thermophilus KCCM 40879
-
-
-
Manually annotated by BRENDA team
Thermus thermophilus KCCM 40879
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-, Q66WM4
uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
malfunction
-
the manA-deficient mutant is unable to utilize D-mannose as a sole carbon source
malfunction
Aspergillus fumigatus YJ-407
-
uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
-
malfunction
Photorhabdus luminescens TT01
-
the manA-deficient mutant is unable to utilize D-mannose as a sole carbon source
-
metabolism
-
the enzyme is part of the biosynthetic pathway of sugar nucleotides essential for welan gum production in Alcaligenes sp., overview
metabolism
-
phosphomannose isomerase catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide synthesis pathway, feedback regulation of this pathway
metabolism
-, Q66WM4
the enzyme catalyzes the first committed step in the synthesis of mannose-containing sugar chains and provides a link between glucose metabolism and mannosylation
metabolism
Alcaligenes sp. CGMCC2428
-
the enzyme is part of the biosynthetic pathway of sugar nucleotides essential for welan gum production in Alcaligenes sp., overview
-
metabolism
Aspergillus fumigatus YJ-407
-
the enzyme catalyzes the first committed step in the synthesis of mannose-containing sugar chains and provides a link between glucose metabolism and mannosylation
-
metabolism
Sphingobium chungbukense DJ77
-
phosphomannose isomerase catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide synthesis pathway, feedback regulation of this pathway
-
physiological function
-
phosphomannose isomerase has a major effect on the formation of a complete, branched extracellular polysaccharide. The manA gene influences biofilm maturation but not initial attachment
physiological function
Photorhabdus luminescens TT01
-
phosphomannose isomerase has a major effect on the formation of a complete, branched extracellular polysaccharide. The manA gene influences biofilm maturation but not initial attachment
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-fructose 6-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
Thermus thermophilus KCCM 40879
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
Q9YE01
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
Q9HIC2
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
-, Q9GRS9
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q9YE01
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q9HIC2
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q5SIM4
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
-, Q9GRS9
first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
Thermus thermophilus KCCM 40879
Q5SIM4
-
-
-
r
D-Fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate
?
show the reaction diagram
-
first enzyme of the N-glycosylation pathway
-
-
-
D-Fructose 6-phosphate
?
show the reaction diagram
Microorganisms
-
mannose 6-phosphate produced in this manner can be incorporated via mannose 1-phosphate as intermediate into guanosine diphosphomannose which participates in numerous processes related to cell wall biosynthesis
-
-
-
D-Fructose 6-phosphate
?
show the reaction diagram
-
enzyme is involved in alginate biosynthesis
-
-
-
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Q9YE01
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Q9HIC2
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Sulfolobus solfataricus P1
-
-
-
-
?
D-Lyxose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Lyxose
D-Xylulose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
D-Lyxose
D-Xylulose
show the reaction diagram
-
38% conversion yield after 3 h
-
-
?
D-Lyxose
D-Xylulose
show the reaction diagram
Thermus thermophilus KCCM 40879
-
-
-
-
r
D-Mannose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Mannose
D-Fructose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Nakazawaea holstii, Microorganisms
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Q9YE01
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Q9HIC2
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-, Q06XM8
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
P25081
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-, Q9AGZ4
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-, Q66WM4
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
beta-D-fructose 6-phosphate serves as substrate in the reverse direction
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
highly specific for the beta anomer of mannose 6-phosphate, the alpha anomer has no activity as a substrate, and is, at best, a poor inhibitor
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Q5SIM4
best substrate
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Pseudomonas aeruginosa PAO1.
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Burkholderia cepacia IST408
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Thermus thermophilus KCCM 40879
Q5SIM4
best substrate
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Sphingobium chungbukense DJ77
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Sulfolobus solfataricus P1
-
-
-
-
?
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Aspergillus fumigatus YJ-407
Q66WM4
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Alcaligenes sp. CGMCC2428
-
-
-
-
r
D-Mannose 6-phosphate
?
show the reaction diagram
Cassia coluteoides
-
enzyme is involved in the utilization of mannose released by hydrolysis of galactomannan on germination after phosphorylation to mannose 6-phosphate
-
-
-
D-Mannose 6-phosphate
?
show the reaction diagram
-
channeling D-mannose 6-phosphate into glycolysis by isomerization to fructose 6-phosphate
-
-
-
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
Thermus thermophilus KCCM 40879
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Thermus thermophilus, Thermus thermophilus KCCM 40879
Q5SIM4
very low activity
-
-
r
D-talose
D-tagatose
show the reaction diagram
-
-
-
-
r
D-talose
D-tagatose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
L-allose
L-psicose
show the reaction diagram
-
-
-
-
r
L-allose
L-psicose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
L-Lyxose
L-Xylulose
show the reaction diagram
-
-
-
-
r
L-Lyxose
L-Xylulose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
L-Lyxose
L-Xylulose
show the reaction diagram
Thermus thermophilus KCCM 40879
-
-
-
-
r
L-Mannose
L-Fructose
show the reaction diagram
-
-
-
-
r
L-Mannose
L-Fructose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
L-Mannose
L-Fructose
show the reaction diagram
Thermus thermophilus KCCM 40879
-
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
-
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
-
29% conversion yield after 3 h
-
-
?
L-ribulose
L-ribose
show the reaction diagram
-
highest activity
-
-
r
L-ribulose
L-ribose
show the reaction diagram
-, Q9AGZ4
best substrate
-
-
r
L-talose
L-tagatose
show the reaction diagram
-
-
-
-
r
L-talose
L-tagatose
show the reaction diagram
-, Q9AGZ4
-
-
-
r
additional information
?
-
-
-
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
-
additional information
?
-
-
adaptive enzyme
-
-
-
additional information
?
-
-
critical role in the supply of the D-mannose derivatives required for many glycosylation reactions
-
-
-
additional information
?
-
-
reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis
-
-
-
additional information
?
-
-
no catalytic activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate
-
-
-
additional information
?
-
-
enzyme substrate specificity with diverse monosaccharide aldoses and ketoses, overview
-
-
-
additional information
?
-
-
Molecular mechanics study of enzyme substrate and inhibitors, overview
-
-
-
additional information
?
-
-
PMI is bifunctional possessing both mannose 6-phosphate isomerase and GDP-mannose diphosphorylase activities
-
-
-
additional information
?
-
-, Q9AGZ4
the enzyme is specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D- and L-enantiomers of ribose, lyxose, talose, mannose, and allose, substrate specificity, overview
-
-
-
additional information
?
-
Thermus thermophilus, Thermus thermophilus KCCM 40879
Q5SIM4
no activity with D-glucose 6-phosphate and arabinose 5-phosphate
-
-
-
additional information
?
-
Sphingobium chungbukense DJ77
-
PMI is bifunctional possessing both mannose 6-phosphate isomerase and GDP-mannose diphosphorylase activities
-
-
-
additional information
?
-
Sulfolobus solfataricus P1
-
no catalytic activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
-, Q9GRS9
first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates
-
r
D-Fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate
?
show the reaction diagram
-
first enzyme of the N-glycosylation pathway
-
-
-
D-Fructose 6-phosphate
?
show the reaction diagram
Microorganisms
-
mannose 6-phosphate produced in this manner can be incorporated via mannose 1-phosphate as intermediate into guanosine diphosphomannose which participates in numerous processes related to cell wall biosynthesis
-
-
-
D-Fructose 6-phosphate
?
show the reaction diagram
-
enzyme is involved in alginate biosynthesis
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
P25081
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-, Q9AGZ4
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
-, Q66WM4
-
-
-
r
D-Mannose 6-phosphate
?
show the reaction diagram
Cassia coluteoides
-
enzyme is involved in the utilization of mannose released by hydrolysis of galactomannan on germination after phosphorylation to mannose 6-phosphate
-
-
-
D-Mannose 6-phosphate
?
show the reaction diagram
-
channeling D-mannose 6-phosphate into glycolysis by isomerization to fructose 6-phosphate
-
-
-
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Sphingobium chungbukense DJ77
-
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Aspergillus fumigatus YJ-407
Q66WM4
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
Alcaligenes sp. CGMCC2428
-
-
-
-
r
additional information
?
-
-
-
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
-
additional information
?
-
-
adaptive enzyme
-
-
-
additional information
?
-
-
critical role in the supply of the D-mannose derivatives required for many glycosylation reactions
-
-
-
additional information
?
-
-
reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-, Q9AGZ4
activates
Ca2+
-
activates
Ca2+
-, Q06XM8
best activator, may be replaced by Mg2+ or Mn2+ for phosphomannose isomerase activity
Ca2+
-, Q9AGZ4
activates
Ca2+
-
activates
Ca2+
Q5SIM4
the enzyme is not stimulated by Ca2+
Co2+
-
can reverse inhibition by EDTA
Co2+
-
can reverse inhibition by a metal binding agent
Co2+
-
best activator
Co2+
-
activates
Co2+
-
required for phosphomannose isomerase activity
Co2+
-, Q9AGZ4
activates, best metal ion, maximal activity at 0.5 mM
Co2+
-
activates, best activator metal ion
Co2+
-
beste metal ion activator
Co2+
-
about 230% activity at 0.5 mM
Cu2+
-, Q9AGZ4
activates
Cu2+
-
maximal activity of the recombinant enzyme for L-ribulose isomerization in the presence of 0.5 mM Cu2+
Cu2+
Q5SIM4
about 135% activity at 0.5 mM
Fe2+
-
can reverse inhibition by EDTA
Fe2+
-
can reverse inhibition by a metal binding agent
Fe2+
Q5SIM4
about 125% activity at 0.5 mM
Mg2+
-
activates
Mg2+
-, Q06XM8
60% of activity with Ca2+ for phosphomannose isomerase activity
Mg2+
P25081
best activating divalent metal ion
Mg2+
-, Q9AGZ4
activates
Mg2+
-
activates only the GMP activity of the enzyme
Mg2+
Q5SIM4
about 175% activity at 0.5 mM
Mn2+
-
can reverse inhibition by a metal binding agent
Mn2+
-
activates
Mn2+
-
activates
Mn2+
-, Q06XM8
65% of activity with Ca2+ for phosphomannose isomerase activity
Mn2+
-, Q9AGZ4
highly activating
Mn2+
-
about 160% activity at 0.5 mM
Ni2+
-
activates
Ni2+
-, Q9AGZ4
activates
Ni2+
-
activates
Zinc
-
contains 1 gatom per mol of enzyme
Zinc
-
enzyme contains an essential zinc atom. Four of the five ligands come from the protein, one of these ligands is unique in that it is a glutamine
Zinc
-
weak activation
Zinc
-
recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
Zn2+
-
can reverse inhibition by EDTA
Zn2+
-
at low concentrations complete reactivation of enzyme inhibited by a metal binding agent
Zn2+
-
activates
Zn2+
-
noncovalent complexation, ESI-FTICR study, binding/release of metal ion changes substrate binding affinity by at least 5fold
Zn2+
P25081
enzyme-bound, Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site
Zn2+
-, Q9AGZ4
activates
Zn2+
-
activates poorly
Zn2+
-
activates
Zn2+
-, Q66WM4
-
Zn2+
-
about 130% activity at 0.5 mM
Zn2+
Q5SIM4
Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+
Zn2+
-
zinc-dependent metalloenzyme
Mn2+
Q5SIM4
about 175% activity at 0.5 mM
additional information
-
activated by bivalent cations in the order: Co2+, Ni2+, Mn2+, Mg2+, Ca2+, Zn2+
additional information
-
activated by bivalent cations in decreasing order: Co2+, Zn2+, Mn2+, Ni2+, Ca2+
additional information
P25081
divalent cations are absolutely required for activity, metal binding increases the thermostability of the enzyme
additional information
-, Q9AGZ4
mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis
additional information
-
the enzyme requires divalent cations for activity
additional information
-
PMI absolutely requires divalent metal cations for catalytic activity
additional information
-
the enzyme is not affected by Ca2+, Mg2+, Ba2+, and Ni2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000041 {5-phospho-D-arabinonohydroxamic acid}
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
0.0006 {5-phospho-D-arabinonhydrazide}
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
2,2'-dipyridyl
-
-
2,3-Butanedione
-
inactivation
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone
-
-
5-deoxy-5-phosphonomethyl-D-arabinonate
-
-
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
-
-
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
-
-
5-phospho-D-arabinonhydrazide
-
-
5-phospho-D-arabinonohydroxamic acid
-
50% inhibition at 0.000169 mM, inhibition of both type I and type II isozymes
5-phospho-D-arabinonohydroxamic acid
-
50% inhibition at 0.000136 mM, inhibition of both type I and type II isozymes
5-phospho-D-arabinonohydroxamic acid
-
nanomolar inhibitor
5-phosphoarabinonate
Q8ZWV0
-
6-deoxy-6-carboxymethyl-D-mannose
-
-
6-deoxy-6-dicarboxymethyl-D-mannose
-
-
6-deoxy-6-dimethylmalonate-D-mannopyranose
-
-
6-deoxy-6-phosphonomethyl-D-mannose
-
-
6-phospho-2-deoxygluconate
Cassia coluteoides
-
competitive
6-phosphogluconate
-
competitive
6-phosphogluconate
Cassia coluteoides
-
slight inhibition
6-phosphogluconate
-
-
6-phosphogluconate
Q9YE01
-
6-phosphogluconate
Q9HIC2
-
6-Phosphomannonate
Cassia coluteoides
-
competitive
8-hydroxyquinoline
-
-
ADP-glucose
-
0.5 mM, 77.8% of initial activity
Ag+
-
irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme
alpha-D-Mannose 6-phosphate
-
poor
Ba2+
Q5SIM4
about 30% inhibition at 0.5 mM
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
-
-
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
-
-
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose
-
-
Cd2+
-
competitive, strongly pH dependent
Cd2+
-
1 mM, no residual activity
D-mannose 1-phosphate
-
0.5 mM, 81.9% of initial activity
diethyldicarbonate
-
-
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
1 mM, 73% residual activity; 1 mM, 84% residual activity
EDTA
-, Q06XM8
2 mM, complete inhibition
EDTA
-
2.5 mM, 54% residual activity; 2.5 mM, 86% residual activity
EDTA
P25081
complete inhibition at 1 mM, reversible by the addition of divalent metal cations such as Zn2+, Mn2+, Co2+, Mg2+ and Ni2+
EDTA
-, Q9AGZ4
complete inactivation
EDTA
-
about 75% residual activity at 0.5 mM
EDTA
Q5SIM4
complete inhibition at 0.5 mM
erythrose 4-phosphate
-
; competitive
erythrose 4-phosphate
Cassia coluteoides
-
D-erythrose 4-phosphate, competitive
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
Q9YE01
-
erythrose 4-phosphate
Q9HIC2
-
Fe2+
-
12% residual activity at 0.5 mM
-
fructose 1-phosphate
-
competitive
Galactose 6-hosphate
-
competitive
-
GDP-D-mannose
-
inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway
GDP-mannose
-
0.5 mM, 46.7% of initial activity
glucosamine 6-phosphate
-
competitive
glucose 1-phosphate
-
competitive
glucose 6-phosphate
-
competitive
Hg2+
-
competitive, relatively pH-independent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion
Hg2+
-
partial noncompetitive inhibition with mannose 6-phosphate as substrate. In addition to the inhibition at rapid equilibrium, inactivation occurs in a two-step process, proceeding via an intermediate complex. The rate of the irreversible inactivation can be slowed by the addition of the substrate mannose 6-phosphate
Hg2+
-
recombinant wild-type enzyme and selenomethionine-labelled enzyme
KI-VALUE
-
-
-
L-ascorbic acid
-
1 mM, 77% residual activity
mannitol 1-phosphate
-
competitive
mannitol 1-phosphate
Cassia coluteoides
-
competitive
p-chloromercuribenzoate
-
0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity
phosphate
-
competitive
ribose 5-phosphate
-
competitive
S-nitroso-acetyl-penicillamine
-
dose- and time-dependent inactivation
Silver sulfadiazine
-
wild-type enzyme is inhibited, mutant enzyme Cys150Ala is not inhibited
Silver sulfadiazine
-
no inhibition
sorbitol 6-phosphate
-
competitive
Zn2+
-
competitive with mannose 6-phosphate, strongly pH-dependent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion
Zn2+
-
inhibitory to both phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
Zn2+
-
1 mM, no residual activity
mannitol 1-phosphate
-
-
additional information
-
no inhibition by N-acetyl-penicillamine
-
additional information
-
not inhibitory: 5-phospho-D-arabinonate
-
additional information
-, Q06XM8
not inhibitory: mannose 1-phosphate, GTP, GDP-mannose, or diphosphate
-
additional information
-
synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive enzyme inhibitors. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview
-
additional information
-
synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive inhibitors of the enzyme. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview
-
additional information
-
no inhibition by GTP, mannose 1-phosphate, and phosphodiphosphate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
Co2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
diphosphate
-
0.5 mM, 120% of initial activity
Mg2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
Mn2+
-
Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
Ni2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00043
-
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
0.33
-
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
0.06
-
D-fructose 6-phosphate
-
pH 7.4, 80C
0.15
-
D-fructose 6-phosphate
-
22C, pH 7.4
0.2
-
D-fructose 6-phosphate
Q9HIC2
80C, pH 7.4
0.21
-
D-fructose 6-phosphate
Q9YE01
50C, pH 7.4
0.22
-
D-fructose 6-phosphate
Q5SIM4
wild type enzyme, pH 7.0, 80C
0.3
-
D-fructose 6-phosphate
-
pH 7.4, 50C
0.44
-
D-fructose 6-phosphate
Q9YE01
80C, pH 7.4
0.002
-
D-glucose 6-phosphate
-
mutant enzyme S309D, at 65C
0.006
-
D-glucose 6-phosphate
-
mutant enzyme S309Q, at 65C
0.008
-
D-glucose 6-phosphate
-
mutant enzyme S309N, at 65C; mutant enzyme S309T, at 65C
0.009
-
D-glucose 6-phosphate
-
mutant enzyme S309A, at 65C
0.012
-
D-glucose 6-phosphate
-
mutant enzyme S309V, at 65C
0.013
-
D-glucose 6-phosphate
-
wild type enzyme, at 65C
0.72
-
D-glucose 6-phosphate
Q9HIC2
80C, pH 7.4
3.5
-
D-glucose 6-phosphate
Q9YE01
80C, pH 7.4
433
-
D-Lyxose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
946
-
D-mannose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
0.0413
-
D-mannose 6-phosphate
-
pH 7.5, 25C
0.06
-
D-mannose 6-phosphate
-
pH 7.4, 80C
0.121
-
D-mannose 6-phosphate
-
pH 7.1, 25C
0.18
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme E132A, pH 7.0, 80C; mutant enzyme E67A, pH 7.0, 80C
0.21
-
D-mannose 6-phosphate
Q5SIM4
wild type enzyme, pH 7.0, 80C
0.25
-
D-mannose 6-phosphate
Q9HIC2
80C, pH 7.4
0.27
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme H122A, pH 7.0, 80C
0.33
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme H50A, pH 7.0, 80C
0.372
-
D-mannose 6-phosphate
-
pH 7.5, 25C
0.53
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme Q48A, pH 7.0, 80C
0.85
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme W13A, pH 7.0, 80C
1.1
-
D-mannose 6-phosphate
Q9YE01
80C, pH 7.4
1.18
-
D-mannose 6-phosphate
-
wild-type, pH 7.0, 25C
1.21
-
D-mannose 6-phosphate
-
22C, pH 7.4
1.29
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme R142A, pH 7.0, 80C
2.5
-
D-mannose 6-phosphate
-
pH 7.1, 25C
9
-
D-mannose 6-phosphate
-, Q06XM8
pH 7.6, presence of 5 mM Mg2+
9.04
-
D-mannose 6-phosphate
-
mutant E410A, pH 7.0, 25C
12.28
-
D-mannose 6-phosphate
-
mutant R479A, pH 7.0, 25C
12.36
-
D-mannose 6-phosphate
-
mutant E458A, pH 7.0, 25C
12.4
-
D-mannose 6-phosphate
-
30C, pH 7.6
12.9
-
D-mannose 6-phosphate
-
mutant N433A, pH 7.0, 25C
15.9
-
D-mannose 6-phosphate
-
mutant R373A, pH 7.0, 25C
16.26
-
D-mannose 6-phosphate
-
mutant H411A, pH 7.0, 25C
23.12
-
D-mannose 6-phosphate
-
mutant R472A, pH 7.0, 25C
110
-
D-ribose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
469
-
D-talose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
312
-
L-allose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
998
-
L-ribose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
136
-
L-ribulose
-
wild type enzyme, at pH 7.0 and 75C
140
-
L-ribulose
-
mutant enzyme R142N, at pH 7.0 and 75C
150
-
L-ribulose
-
mutant enzyme R142Q, at pH 7.0 and 75C
151
-
L-ribulose
-
mutant enzyme R142E, at pH 7.0 and 75C
184
-
L-ribulose
-
mutant enzyme R142A, at pH 7.0 and 75C
228
-
L-ribulose
-
mutant enzyme R142K, at pH 7.0 and 75C
308
-
L-ribulose
-
mutant enzyme R142Y, at pH 7.0 and 75C
0.17
-
mannose 6-phosphate
-
-
0.2
-
mannose 6-phosphate
-
Hepes buffer
0.23
-
mannose 6-phosphate
-
recombinant enzyme
0.25
-
mannose 6-phosphate
-
wild-type enzyme
0.65
-
mannose 6-phosphate
-
-
0.73
-
mannose 6-phosphate
-
-
0.8
-
mannose 6-phosphate
-
selenomethionine-labelled enzyme, Hepes buffer
1
-
mannose 6-phosphate
-
Tris/HCl buffer
1.24
-
mannose 6-phosphate
-
-
1.35
-
mannose 6-phosphate
-
-
1.6
-
mannose 6-phosphate
Cassia coluteoides
-
enzyme from developing seeds
1.9
-
mannose 6-phosphate
Cassia coluteoides
-
enzyme from germinating seeds
2
-
mannose 6-phosphate
-
-
3.03
-
mannose 6-phosphate
-
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase
4
-
mannose 6-phosphate
-
selenomethionine-labelled enzyme, Tris/HCl buffer
additional information
-
additional information
-
enzyme kinetics with D-lyxose and L-ribose, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
6
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
23
-
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
141
-
D-fructose 6-phosphate
Q5SIM4
wild type enzyme, pH 7.0, 80C
7089
-
D-Lyxose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
3748
-
D-mannose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
0.076
-
D-mannose 6-phosphate
-
pH 7.1, 25C
0.25
-
D-mannose 6-phosphate
-
mutant R472A, pH 7.0, 25C
0.54
-
D-mannose 6-phosphate
-
mutant R479A, pH 7.0, 25C
0.75
-
D-mannose 6-phosphate
-
mutant R373A, pH 7.0, 25C
1.38
-
D-mannose 6-phosphate
-
wild-type, pH 7.0, 25C
2.63
-
D-mannose 6-phosphate
-
mutant E410A, pH 7.0, 25C
3.25
-
D-mannose 6-phosphate
-
mutant E458A, pH 7.0, 25C
3.5
-
D-mannose 6-phosphate
-
mutant N433A, pH 7.0, 25C
4.41
-
D-mannose 6-phosphate
-
mutant H411A, pH 7.0, 25C
11
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme W13A, pH 7.0, 80C
19
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme E132A, pH 7.0, 80C
19.4
-
D-mannose 6-phosphate
-, Q06XM8
pH 7.6, presence of 5 mM Mg2+
20
-
D-mannose 6-phosphate
-
pH 7.1, 25C
31
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme E67A, pH 7.0, 80C
37
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme Q48A, pH 7.0, 80C
54
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme H50A, pH 7.0, 80C
70
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme R142A, pH 7.0, 80C
75
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme H122A, pH 7.0, 80C
1371
-
D-mannose 6-phosphate
Q5SIM4
wild type enzyme, pH 7.0, 80C
72
-
D-ribose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
63970
-
D-talose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
920
-
L-allose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
17600
-
L-ribose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
32670
-
L-ribulose
-
mutant enzyme R142E, at pH 7.0 and 75C
48300
-
L-ribulose
-
mutant enzyme R142Q, at pH 7.0 and 75C
50640
-
L-ribulose
-
wild type enzyme, at pH 7.0 and 75C
56180
-
L-ribulose
-
mutant enzyme R142Y, at pH 7.0 and 75C
64870
-
L-ribulose
-
mutant enzyme R142A, at pH 7.0 and 75C
68880
-
L-ribulose
-
mutant enzyme R142K, at pH 7.0 and 75C
81060
-
L-ribulose
-
mutant enzyme R142N, at pH 7.0 and 75C
121
-
mannose 6-phosphate
-
selenomethionine-labelled enzyme
162
-
mannose 6-phosphate
-
wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
70
-
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0
840
-
beta-D-mannose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0
641
-
D-fructose 6-phosphate
Q5SIM4
wild type enzyme, pH 7.0, 80C
9143
16.4
-
D-Lyxose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
9268
3.5
-
D-mannose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
9286
13
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme W13A, pH 7.0, 80C
9288
54
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme R142A, pH 7.0, 80C
9288
69
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme Q48A, pH 7.0, 80C
9288
109
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme E132A, pH 7.0, 80C
9288
166
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme H50A, pH 7.0, 80C
9288
174
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme E67A, pH 7.0, 80C
9288
278
-
D-mannose 6-phosphate
Q5SIM4
mutant enzyme H122A, pH 7.0, 80C
9288
6685
-
D-mannose 6-phosphate
Q5SIM4
wild type enzyme, pH 7.0, 80C
9288
0.6
-
D-ribose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
9348
6.8
-
D-talose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
9377
2.9
-
L-allose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
271994
17.6
-
L-ribose
-, Q9AGZ4
pH 7.5, 40C, recombinant enzyme
80181
182
-
L-ribulose
-
mutant enzyme R142Y, at pH 7.0 and 75C
12394
216
-
L-ribulose
-
mutant enzyme R142E, at pH 7.0 and 75C
12394
302
-
L-ribulose
-
mutant enzyme R142K, at pH 7.0 and 75C
12394
322
-
L-ribulose
-
mutant enzyme R142Q, at pH 7.0 and 75C
12394
353
-
L-ribulose
-
mutant enzyme R142A, at pH 7.0 and 75C
12394
374
-
L-ribulose
-
wild type enzyme, at pH 7.0 and 75C
12394
579
-
L-ribulose
-
mutant enzyme R142N, at pH 7.0 and 75C
12394
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0006
-
5-phospho-D-arabinonhydrazide
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0.002
-
5-phospho-D-arabinonhydrazide
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0.000041
-
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0.00008
-
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0.000086
-
5-phospho-D-arabinonohydroxamic acid
-
pH 7.1, 25C
0.000137
-
5-phospho-D-arabinonohydroxamic acid
-
pH 7.1, 25C
0.0105
-
6-deoxy-6-dicarboxymethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
0.115
-
6-deoxy-6-dicarboxymethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
0.11
-
6-phosphogluconate
-
pH 7.4, 50C
2
10
6-phosphogluconate
Q9HIC2
80C, pH 7.4
58
-
6-phosphogluconate
Q9YE01
80C, pH 7.4
0.035
-
erythrose 4-phosphate
Q9YE01
80C, pH 7.4
0.164
-
erythrose 4-phosphate
Q9HIC2
80C, pH 7.4
0.0014
-
erythrose-4-phosphate
-
pH 7.4, 50C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
-
5-deoxy-5-phosphonomethyl-D-arabinonate
-
above, pH 7.1, 25C, recombinant enzyme
3
-
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
-
above, pH 7.1, 25C, recombinant enzyme
0.37
-
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
-
pH 7.1, 25C, recombinant enzyme
2.2
-
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
-
pH 7.1, 25C, recombinant enzyme
0.9
-
6-deoxy-6-carboxymethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
4.6
-
6-deoxy-6-carboxymethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
0.0181
-
6-deoxy-6-dicarboxymethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
0.199
-
6-deoxy-6-dicarboxymethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
1.61
-
6-deoxy-6-phosphonomethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
4.7
-
6-deoxy-6-phosphonomethyl-D-mannose
-
pH 7.1, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.01
-
Q5SIM4
wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80C
0.0101
-
-, Q9AGZ4
recombinant enzyme
0.0165
-
-, Q9AGZ4
recombinant enzyme
0.0225
-
-, Q9AGZ4
recombinant enzyme
0.0659
-
-, Q9AGZ4
recombinant enzyme
0.0918
-
-, Q9AGZ4
recombinant enzyme
0.269
-
-
enzyme activity in cells after 54 h growth on maltose
0.3
-
Q5SIM4
mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
0.306
-
-
enzyme activity in cells after 54 h growth on sucrose
0.313
-
-
enzyme activity in cells after 54 h growth on glucose
0.6
-
Q5SIM4
mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
0.74
-
Q5SIM4
wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80C
1.4
-
Q5SIM4
mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
1.5
-
Q5SIM4
mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
1.7
-
Q5SIM4
mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
1.9
-
Q5SIM4
mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
2.1
-
Q5SIM4
mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
2.8
-
Q5SIM4
mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
3
8
Q5SIM4
mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
3
-
-
wild type enzyme, using D-psicose as substrate, at pH 7.0 and 75C
4.5
-
Q5SIM4
wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80C
11
-
Q5SIM4
mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
16
-
-
wild type enzyme, using L-tagatose as substrate, at pH 7.0 and 75C
16
-
Q5SIM4
mutant enzyme K37A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
19
-
-
wild type enzyme, using L-mannose as substrate, at pH 7.0 and 75C
22
-
-
wild type enzyme, using L-xylulose as substrate, at pH 7.0 and 75C
23
-
-
wild type enzyme, using L-lyxose as substrate, at pH 7.0 and 75C
31
-
Q5SIM4
mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
39
-
Q5SIM4
mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
40
-
Q5SIM4
mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
42
-
-
wild type enzyme, using L-psicose as substrate, at pH 7.0 and 75C
44
-
Q5SIM4
mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
51
-
Q5SIM4
mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
57
-
-
wild type enzyme, using L-fructose as substrate, at pH 7.0 and 75C
58
-
-
wild type enzyme, using D-ribose as substrate, at pH 7.0 and 75C
58
-
Q5SIM4
mutant enzyme L18A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
63
-
-
wild type enzyme, using L-talose as substrate, at pH 7.0 and 75C
75
-
-
-
75
-
Q5SIM4
wild type enzyme, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
80
-
-
-
85
-
-
wild type enzyme, using D-tagatose as substrate, at pH 7.0 and 75C
126
-
-
wild type enzyme, using D-ribulose as substrate, at pH 7.0 and 75C
128
-
-
wild type enzyme, using D-xylulose as substrate, at pH 7.0 and 75C
165
-
-
wild type enzyme, using D-allose as substrate, at pH 7.0 and 75C
167
-
-
wild type enzyme, using D-fructose as substrate, at pH 7.0 and 75C
194
-
Q5SIM4
mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
333
-
-
wild type enzyme, using D-lyxose as substrate, at pH 7.0 and 75C
425
-
-
wild type enzyme, using L-ribose as substrate, at pH 7.0 and 75C
474
-
-
mutant enzyme K37A, using L-ribulose as substrate, at pH 7.0 and 75C
742
-
-
wild type enzyme, using L-allose as substrate, at pH 7.0 and 75C
838
-
-
mutant enzyme W13A, using L-ribulose as substrate, at pH 7.0 and 75C
842
-
-
wild type enzyme, using D-mannose as substrate, at pH 7.0 and 75C
890
-
-
purified recombinant enzyme
972
-
-
mutant enzyme D138A, using L-ribulose as substrate, at pH 7.0 and 75C
1011
-
-
mutant enzyme K65A, using L-ribulose as substrate, at pH 7.0 and 75C
1016
-
-
mutant enzyme Q48A, using L-ribulose as substrate, at pH 7.0 and 75C
1045
-
-
mutant enzyme R142E, using L-ribulose as substrate, at pH 7.0 and 75C
1046
-
-
mutant enzyme W69A, using L-ribulose as substrate, at pH 7.0 and 75C
1065
-
-
mutant enzyme L39A, using L-ribulose as substrate, at pH 7.0 and 75C
1076
-
-
mutant enzyme L124A, using L-ribulose as substrate, at pH 7.0 and 75C
1092
-
-
mutant enzyme R142Y, using L-ribulose as substrate, at pH 7.0 and 75C
1194
-
-
mutant enzyme L18A, using L-ribulose as substrate, at pH 7.0 and 75C
1214
-
-
mutant enzyme R142K, using L-ribulose as substrate, at pH 7.0 and 75C
1270
-
-
mutant enzyme R142Q, using L-ribulose as substrate, at pH 7.0 and 75C
1482
-
-
mutant enzyme R11A, using L-ribulose as substrate, at pH 7.0 and 75C
1493
-
-
wild type enzyme, using L-ribulose as substrate, at pH 7.0 and 75C
1619
-
-
wild type enzyme, using D-talose as substrate, at pH 7.0 and 75C
1791
-
-
mutant enzyme R142A, using L-ribulose as substrate, at pH 7.0 and 75C
2152
-
-
mutant enzyme R14N, using L-ribulose as substrate, at pH 7.0 and 75C
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
mass spectrometry based method for the direct determination of kinetic konstants of enzyme
additional information
-
-, Q9AGZ4
substrate specificity, overview
additional information
-
-
enzyme activity and metabolic parameters in different tissue at different reproductive stages in female and male animals, PMI shows no variability, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
Cassia coluteoides
-
-
7
-
-
maximal activity of the recombinant enzyme for L-ribulose isomerization
7.5
-
-, Q9AGZ4
recombinant enzyme
7.6
-
-
assay at
7.6
-
-, Q66WM4
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9
-
about 50% of maximal activity at pH 5.5 and pH 9.0
6
11
Cassia coluteoides
-
pH 6.0: 50% of maximal activity, relative high activity up to pH 11
6.3
8.8
-
more than 50% of maximum activity in this range
6.5
8.5
-, Q9AGZ4
-
6.5
8.5
Q5SIM4
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
P25081
assay at room temperature
37
-
-, Q66WM4
assay at
40
-
-, Q9AGZ4
recombinant enzyme
75
-
-
maximal activity of the recombinant enzyme for L-ribulose isomerization
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
-, Q9AGZ4
-
70
90
Q5SIM4
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
-
calculated
6
-
-, Q06XM8
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
growth on liquid and solid media, but no in presence of 90 mM mannose. After transfer of sucrose-grown cell onto medium containing mannose, cells grew little initially, but after a month lag period, they start to form callus colonies. Mannose-accomodated cells are capable of converting mannose to sucrose, with enhanced phosphomannose isomerase activity
Manually annotated by BRENDA team
Cassia coluteoides
-
developing and germinating
Manually annotated by BRENDA team
-
induction of expression under continuous light. Diurnal expression pattern in parallel with the total Pmi1 activity and the total ascorbic acid content in leaf
Manually annotated by BRENDA team
additional information
-
constitutive expression in both vegetative and reproductive organs; no expression in any organ under light. Under long term darkness, expression of isoform Pmi2 with concomitant decrease in ascorbic acid levels
Manually annotated by BRENDA team
additional information
-
enzyme activity and metabolic parameters in different tissue at different reproductive stages in female and male animals, PMI shows no variability, overview
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29000
-
-
gel filtration
29100
-
Q5SIM4
gel filtration
36000
-
-
gel filtration, recombinant enzyme
36600
-
-, Q9AGZ4
gel filtration, recombinant enzyme
45000
-
-
gel filtration
45000
-
Q9YE01
gel filtration
46520
-
-
calculation from nucleotide sequence encoded by cDNA
46530
-
-
recombinant enzyme, electrospray mass spectroscopy
48000
-
Q9HIC2
gel filtration
48740
-
-
wild-type recombinant enzyme, electrospray mass spectroscopy
49060
-
-
selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy
53000
-
-
SDS-PAGE
54000
-
-
gel filtration
54000
-
-
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase, gel filtration
58000
-
-
gel filtration
59000
-
-
gel filtration
63000
-
-
gel filtration
65000
-
-
sedimentation equilibrium, analytical ultracentrifugation
67000
-
Cassia coluteoides
-
enzyme from seeds, gel filtration
67000
-
Q9HIC2
analytical ultracentrifugation
68000
-
Cassia coluteoides
-
enzyme from pods, gel filtration
74500
-
Cassia coluteoides
-
enzyme from pods and seeds, density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 56000, SDS-PAGE
?
-
x * 61000, calculation from nucleotide sequence
?
-, Q06XM8
x * 55300, calculated, x * 55000, SDS-PAGE
?
-
x * 55716, calculated, x * 56000, SDS-PAGE
?
-
x * 50000, recombinant His6-tagged enzyme, SDS-PAGE
?
Burkholderia cepacia IST408
-
x * 55300, calculated, x * 55000, SDS-PAGE
-
?
Sphingobium chungbukense DJ77
-
x * 50000, recombinant His6-tagged enzyme, SDS-PAGE
-
dimer
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
dimer
Q9YE01
2 * 36000, SDS-PAGE, 2 * 36100, calculated
dimer
Q9HIC2
2 * 35000, SDS-PAGE, 2 * 35150, calculated
monomer
-
1 * 56000, bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-, Q9AGZ4
* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation
monomer
-
1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 36452, sequence calculation
monomer
-
1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence
monomer
Thermus thermophilus KCCM 40879
-
1 * 29000, SDS-PAGE; 1 * 29000, SDS-PAGE; 1 * 29054, calculated from amino acid sequence; 1 * 29054, calculated from amino acid sequence
-
additional information
-
bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is composed of two independent enzymatic domains. The carboxyl terminus is critical for mannose-6-phosphate isomerase
additional information
-
PMI possesses two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus
additional information
Sphingobium chungbukense DJ77
-
PMI possesses two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
homology modeling of structure and refinement by energy minimization and molecular dynamics
-
both in complex with fructose 6-phosphate and with glucose 6-phosphate
-, Q8ZWV0
both native form and in complex with 5-phosphoarabinonate
Q8ZWV0
enzyme in apoform without metal ion, in the holoform with bound Zn2+, or complexed with bound inhibitor yttrium, or with Zn2+ and fructose 6-phosphate, microbatch method, 0.003 ml of protein solution and crystallization solution are mixed containing 4 mg/ml protein, 0.1 M magnesium acetate, 0.2 M sodium cacodylate, pH 6.5, 20% PEG 8000 and 5% dioxane, addition of 10 mM metal ions and 250 mM fructose 6-phosphate for complexed enzyme, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement
P25081
to 1.66 A resolution, space group P212121. Preliminary structure solution by molecular replacement using the strucutre from Candida albicans mannose-6-phosphate isomerase
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
40C, 1 h, about 35% loss of activity
6
9.5
-
40C, 1 h, no loss of activity
6.5
8
-
4C, stable
10
-
-
40C, 1 h, about 25% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-, Q9AGZ4
purified recombinant enzyme, half-life is 461 h
28
-
-
half-life in absence of Zn2+: 110 min, half-life in presence of 0.0002 mM ZnCl2: 270 min
30
-
-, Q9AGZ4
purified recombinant enzyme, half-life is 325 h
35
-
-, Q9AGZ4
purified recombinant enzyme, half-life is 236 h
37
-
-
6 min, wild-type enzyme stable, mutant enzyme loses about 90% of activity
40
-
-
pH 10, about 25% loss of activity; pH 5.5, 1 h, about 35% loss of activity; pH 6.0-9.5, 1 h, no loss of activity
40
-
-, Q9AGZ4
purified recombinant enzyme, half-life is 111 h
45
-
-
pH 6.5, 30 min, native enzyme stable
45
-
-, Q9AGZ4
purified recombinant enzyme, half-life is 56 h
50
-
-, Q9AGZ4
purified recombinant enzyme, half-life is 10 h
55
-
-
pH 6.5, 10 min, about 75% loss of native enzyme
60
-
-
enzyme half-life is 388 h
64
85
Q5SIM4
the half-lives of the enzyme at 65, 70, 75, 80, and 85C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively
65
85
-
the enzyme shows half-lives of 22, 10, 5.5, 2.1, and 0.3 h at 65, 70, 75, 80, and 85C, respectively
65
-
-
enzyme half-life is 73 h
70
-
-
enzyme half-life is 27 h
100
-
-
melting temperature for thermal unfolding, 60 min, 50% residual activity
additional information
-
-, Q9AGZ4
first-order kinetics for thermal inactivation
additional information
-
-
thermal inactivation of GTMpi follows first-order kinetics
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
EDTA-treated enzyme and 1,10-phenanthroline-treated enzyme is more susceptible to heat denaturation, addition of various metal ions causes the recovery of thermal stability. The most effective metal ion is Co2+, which causes the recovery of thermal stability to a level higher than that of the native enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, unstable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme 27fold from Escherichia coli strain ER2566 by affinity chromatography
-, Q9AGZ4
normal and selenomethionine-labelled enzyme expressed in Escherichia coli
-
recombinant enzyme 8.7fold from Escherichia coli strain ER2566
-
HiTrap Ni-chelating column chromatography and Q-Sepharose column chromatography
-
Ni-affinity column
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
P25081
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
HisTrap HP column chromatography
Q5SIM4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Agrobacterium tumefaciens
Q9M884
expression in Escherichia coli
-
expression in Escherichia coli strain ER2566
-, Q9AGZ4
expression in Escherichia coli
-
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli
-
Agrobacterium-based expression in Linum usitatissimum
-
expression in Brassica rapa
-
expression in Pseudomonas aeruginosa
-
use of enzyme as selectable marker
-
expression in Escherichia coli strain ER2566
-
expression in Escherichia coli strain ER2566, coexpression with L-arabinose isomerase
-
cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coli
-
expressed in Escherichia coli GI724 cells
-
high level expression in Escherichia coli M15 as inclusion bodies
-, Q9GRS9
overexpressed under the control of the tac promoter in the broad-host-range controlled-expression vector pMMB22, expression in Escherichia coli
-
overexpression in both mucoid and nonmucoid strains of Pseudomonas aeruginosa
-
expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain
-
overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
P25081
gene pmi, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli ER2566 cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E410A
-
about 25% of wild-type catalytic efficiency
E458A
-
about 25% of wild-type catalytic efficiency
N433A
-
about 25% of wild-type catalytic efficiency
R373A
-
about 4% of wild-type catalytic efficiency
R408A
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R408K
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R472A
-
about 1% of wild-type catalytic efficiency
R479A
-
about 3% of wild-type catalytic efficiency
E410A
Pseudomonas aeruginosa PAO1.
-
about 25% of wild-type catalytic efficiency
-
H411A
Pseudomonas aeruginosa PAO1.
-
about 25% of wild-type catalytic efficiency
-
R408A
Pseudomonas aeruginosa PAO1.
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
-
R408K
Pseudomonas aeruginosa PAO1.
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
-
S309A
-
42% decreased activity compared to the wild type enzyme
S309D
-
96% decreased activity compared to the wild type enzyme
S309N
-
73% decreased activity compared to the wild type enzyme
S309Q
-
78% decreased activity compared to the wild type enzyme
S309T
-
64% decreased activity compared to the wild type enzyme
S309V
-
64% decreased activity compared to the wild type enzyme
S309A
Sulfolobus solfataricus P1
-
42% decreased activity compared to the wild type enzyme
-
S309N
Sulfolobus solfataricus P1
-
73% decreased activity compared to the wild type enzyme
-
S309Q
Sulfolobus solfataricus P1
-
78% decreased activity compared to the wild type enzyme
-
S309T
Sulfolobus solfataricus P1
-
64% decreased activity compared to the wild type enzyme
-
S309V
Sulfolobus solfataricus P1
-
64% decreased activity compared to the wild type enzyme
-
D138A
-
the enzyme shows decreased specific activity for L-ribulose
D138A
Q5SIM4
the mutant shows 59% activity compared to the wild type enzyme
E132A
-
the mutants has no activity for L-ribulose
E132A
Q5SIM4
the mutant shows 1.9% activity compared to the wild type enzyme
E132D
Q5SIM4
the mutant shows 0.4% activity compared to the wild type enzyme
E132K
Q5SIM4
inactive
E132Q
Q5SIM4
inactive
E132W
Q5SIM4
inactive
E67A
-
the mutants has no activity for L-ribulose
E67A
Q5SIM4
the mutant shows 2.5% activity compared to the wild type enzyme
E67D
Q5SIM4
the mutant shows 3.7% activity compared to the wild type enzyme
E67K
Q5SIM4
inactive
E67Q
Q5SIM4
the mutant shows 0.8% activity compared to the wild type enzyme
E67W
Q5SIM4
inactive
H122A
-
the mutants has no activity for L-ribulose
H122A
Q5SIM4
the mutant shows 2.8% activity compared to the wild type enzyme
H122D
Q5SIM4
inactive
H122K
Q5SIM4
inactive
H122Q
Q5SIM4
the mutant shows 2.0% activity compared to the wild type enzyme
H122W
Q5SIM4
inactive
H50A
-
the mutants has no activity for L-ribulose
H50A
Q5SIM4
the mutant shows 2.2% activity compared to the wild type enzyme
H50D
Q5SIM4
inactive
H50K
Q5SIM4
inactive
H50Q
Q5SIM4
the mutant shows 2.0% activity compared to the wild type enzyme
H50W
Q5SIM4
inactive
K37A
-
the enzyme shows decreased specific activity for L-ribulose
K37A
Q5SIM4
the mutant shows 21% activity compared to the wild type enzyme
K65A
-
the enzyme shows decreased specific activity for L-ribulose
K65A
Q5SIM4
the mutant shows 15% activity compared to the wild type enzyme
L124A
-
the enzyme shows decreased specific activity for L-ribulose
L18A
-
the enzyme shows decreased specific activity for L-ribulose
L18A
Q5SIM4
the mutant shows 78% activity compared to the wild type enzyme
L39A
-
the enzyme shows decreased specific activity for L-ribulose
L39A
Q5SIM4
the mutant shows 84% activity compared to the wild type enzyme
Q48A
-
the enzyme shows decreased specific activity for L-ribulose
Q48A
Q5SIM4
the mutant shows 2.0% activity compared to the wild type enzyme
Q48D
Q5SIM4
inactive
Q48K
Q5SIM4
inactive
Q48N
Q5SIM4
inactive
Q48W
Q5SIM4
inactive
R11A
-
the enzyme shows about wild type specific activity for L-ribulose
R11A
Q5SIM4
the mutant shows 260% activity compared to the wild type enzyme
R142A
-
the enzyme shows increased specific activity for L-ribulose
R142A
Q5SIM4
the mutant shows 2.6% activity compared to the wild type enzyme
R142D
Q5SIM4
inactive
R142E
-
the enzyme shows decreased specific activity for L-ribulose
R142K
-
the enzyme shows decreased specific activity for L-ribulose
R142K
Q5SIM4
inactive
R142N
-
the specific activity and catalytic efficiency (kcat/Km) for L-ribulose using the R142N mutant are 1.4 and 1.6fold higher than those of the wild type enzyme, respectively
R142N
Q5SIM4
inactive
R142Q
-
the enzyme shows decreased specific activity for L-ribulose
R142W
Q5SIM4
inactive
R142Y
-
the enzyme shows decreased specific activity for L-ribulose
W13A
-
the enzyme shows decreased specific activity for L-ribulose
W13A
Q5SIM4
the mutant shows 0.4% activity compared to the wild type enzyme
W13D
Q5SIM4
inactive
W13F
Q5SIM4
the mutant shows 41% activity compared to the wild type enzyme
W13H
Q5SIM4
the mutant shows 52% activity compared to the wild type enzyme
W13K
Q5SIM4
inactive
W13Q
Q5SIM4
inactive
W13Y
Q5SIM4
the mutant shows 68% activity compared to the wild type enzyme
W69A
-
the enzyme shows decreased specific activity for L-ribulose
W69A
Q5SIM4
the mutant shows 50% activity compared to the wild type enzyme
Y124A
Q5SIM4
the mutant shows 52% activity compared to the wild type enzyme
E132A
Thermus thermophilus KCCM 40879
-
the mutants has no activity for L-ribulose; the mutant shows 1.9% activity compared to the wild type enzyme
-
E132D
Thermus thermophilus KCCM 40879
-
the mutant shows 0.4% activity compared to the wild type enzyme
-
E132Q
Thermus thermophilus KCCM 40879
-
inactive
-
H122A
Thermus thermophilus KCCM 40879
-
the mutants has no activity for L-ribulose; the mutant shows 2.8% activity compared to the wild type enzyme
-
K37A
Thermus thermophilus KCCM 40879
-
the enzyme shows decreased specific activity for L-ribulose; the mutant shows 21% activity compared to the wild type enzyme
-
R11A
Thermus thermophilus KCCM 40879
-
the enzyme shows about wild type specific activity for L-ribulose
-
R142K
Thermus thermophilus KCCM 40879
-
the enzyme shows decreased specific activity for L-ribulose
-
additional information
-
knockout of isoform Pmi2 does not affect the total ascorbic acid levels in leaves; reduction of Pmi1 expression by RNA interference results in substantial decrease in the total ascorbic acid content of leaves
additional information
-, Q66WM4
construction of a DELTApmi1 enzyme knockout mutant cell, that shows a significantly reduced growth rate at a high concentration of Man. Both inadequate and replete Man leads to an accumulation of intracellular Man-6-P and a reduction in the amount of alpha-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
additional information
Aspergillus fumigatus YJ-407
-
construction of a DELTApmi1 enzyme knockout mutant cell, that shows a significantly reduced growth rate at a high concentration of Man. Both inadequate and replete Man leads to an accumulation of intracellular Man-6-P and a reduction in the amount of alpha-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
-
additional information
-
transformation of Brassica napus with gene pmi as a selectable marker, transformation via Agrobacterium tumefaciens in hypocotyl explants, overview
additional information
-, Q06XM8
enzyme-deficient mutant is not impaired in synthesis of exopolysaccharide. However, the viscosity of aqueous solutions prepared with the exopolysaccharide produced by the mutant is significantly reduced compared with wild-type biopolymer and the mutant forms biofilms with a size reduced by 6fold
additional information
Burkholderia cepacia IST408
-
enzyme-deficient mutant is not impaired in synthesis of exopolysaccharide. However, the viscosity of aqueous solutions prepared with the exopolysaccharide produced by the mutant is significantly reduced compared with wild-type biopolymer and the mutant forms biofilms with a size reduced by 6fold
-
C150A
-
mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition
additional information
-
ablation of enzyme gene, homozygous embryos die around E11.5. Supplementation with D-mannose hastened their death. Embryos show growth retardation and placental hyperplasia. More than 90% of embryos failed to form yolk sac vasculature, and 35% failed chorioallantoic fusion
H411A
-
about 25% of wild-type catalytic efficiency
additional information
-
point mutation at nucleotide 961 greatly decreases enzyme activity
R479A
Pseudomonas aeruginosa PAO1.
-
about 3% of wild-type catalytic efficiency
-
additional information
-
thermolabile mutant enzyme
additional information
-
enzyme deleltion strain, cells are viable only if supplemented with extracellular mannose and glucose. Increase of extracellular mannose concentration results in significantly reduced growth rates without alterations in intracellular GDP-mannose levels and in increase of mannose 6-phosphate levels
additional information
-
inactivation of the manA gene encoding phosphomannose isomerase results in production of amphotericins and their aglycones, 8-deoxyamphoteronolides. A double mutant lacking the phosphomannose isomerase and phosphomannomutase genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-, Q9AGZ4
mannose-6-phosphate isomerase from Bacillus subtilis is applied for the production of L-ribose by direct isomerization of L-ribulose
analysis
-
development and optimization of a transformation method using the phosphomannose-isomerase gene pmi as a selectable marker for Brassica napus transformation via Agrobacterium tumefaciens, overview
pharmacology
-
absence of mannose-6-phosphate isomerase causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs
agriculture
-
non-antibiotic selection system based on heterologous expression of enzyme in Brassica rapa via Agrobacterium tumefaciens infection and screening for cotyledon explants that survive in media containing more than 5 g per l mannose. Presence of gene does not inhibit the growth of transgenic plants
agriculture
-
expression system based on phosphomannose-isomerase gene as a selectable marker in Agrobacterium-based transformation and mannose as the selective agent for the transformation of apple. Selection of leaf explants on medium supplemented with mannose and sorbitol, integration of transgenes in the apple genome and their activity are confirmed
agriculture
-
selection system for onion using Agrobacterium-based transformation with phosphomannose isomerase as selectable marker. Selection depends on detoxification of mannose 6-phosphate by conversion to fructose 6-phosphate in six-week-old embryonic calli. Transformation rates of 23-27% are obtained
agriculture
-
use of enzyme as selectable marker in Agrobacterium-based expression of transgenes in Brassica rapa. Supplementation of media with 7 g per l mannose and 2% sucrose provides best conditions for the selection of transformed plants. Transformation rates of 1.4-3% are obtained
agriculture
-
use of enzyme as selectable marker for Agrobacterium-medated transformation of Linum usitatissimum. Transgenic flax plants able to root on mannose-containing medium are obtained on a combination of 20 g per l sucrose and 10 g per l mannose. Mean transformation efficacy is 3.6%
biotechnology
-
use of enzyme gene as selectable marker for transformation of Penniseum glaucum. Enzyme gene is a superior selectable marker for improving transformation efficiencies when compared to antibiotic or herbicide selectable marker genes
biotechnology
-
effective use of enzyme gene as selectable marker gene for transformation of embryogenic calli of Carica papaya
biotechnology
-
selection system for transformation of onion using enzyme gene and Agrobacterium. Transformation rates are around 25%
biotechnology
-
use of enzyme as selectable marker for transformation of Oriza sativa immature embryo via Agrobacterium
synthesis
-
L-ribose production of the enzyme in a coupled assay system with L-arabinose isomerase, EC 5.3.1.4, in recombinant Escherichia coli ER2566, AI/MPI ratio, 1:2.5, method optimization. L-Ribose is a potential starting material for the synthesis of many L-nucleoside-based pharmaceutical compounds
pharmacology
-, Q9GRS9
the enzyme may be a target for anti-Leishmania drug development
biotechnology
Oncidium Gower Ramsey, Oncidium sp.
-
the pmi/mannose selection system is highly efficient for producing transgenic Oncidium Gower Ramsey without using antibiotics or herbicides
synthesis
-
inactivation of the manA gene encoding phosphomannose isomerase results in production of amphotericins and their aglycones, 8-deoxyamphoteronolides. A double mutant lacking the phosphomannose isomerase and phosphomannomutase genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins